You Searched For: Riboflavine+(Vitamin+B2)

Catalog Number: (BOSSBS-7762R-A647)

Supplier: Bioss

Description: Factor Xa is a vitamin K-dependent glycoprotein that converts prothrombin to thrombin in the presence of factor Va, calcium and phospholipid during blood clotting.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-3900R-HRP)

Supplier: Bioss

Description: CYP2R1 is a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are mono-oxygenases which catalyze many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This enzyme is a microsomal vitamin D hydroxylase that converts vitamin D into the active ligand for the vitamin D receptor.Defects in CYP2R1 are a cause of 25-hydroxyvitamin D(3) deficiency, also known as pseudovitamin D(3) deficiency rickets due to 25-hydroxylase deficiency. First described in patients who had rickets at a young age despite a history of adequate vitamin D intake. The patients sera had low calcium concentrations, low phosphate concentrations, elevated alkaline phosphatase activity and low levels of 25-hydroxyvitamin D.

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Catalog Number: (BOSSBS-3900R-A680)

Supplier: Bioss

Description: CYP2R1 is a member of the cytochrome P450 superfamily of enzymes. The cytochrome P450 proteins are mono-oxygenases which catalyse many reactions involved in drug metabolism and synthesis of cholesterol, steroids and other lipids. This enzyme is a microsomal vitamin D hydroxylase that converts vitamin D into the active ligand for the vitamin D receptor.Defects in CYP2R1 are a cause of 25-hydroxyvitamin D(3) deficiency, also known as pseudovitamin D(3) deficiency rickets due to 25-hydroxylase deficiency. First described in patients who had rickets at a young age despite a history of adequate vitamin D intake. The patients sera had low calcium concentrations, low phosphate concentrations, elevated alkaline phosphatase activity and low levels of 25-hydroxyvitamin D.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-6336R-CY5)

Supplier: Bioss

Description: APOB48R is a macrophage receptor that binds to the apolipoprotein B48 of dietary triglyceride (TG) rich lipoproteins. It may provide essential lipids, lipid soluble vitamins and other nutrients to reticuloendothelial cells.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-10342R-A750)

Supplier: Bioss

Description: In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunit have been identified, designated PP1, PP2A, PP2B and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4), is a putative member of a novel PP family. The PP2B family comprises subfamily members PP2B-A alpha, PP2B-A Beta and PP2B-A Gamma. Two additional regulatory subunits been identified, designated PP2B-B1 and PP2B-B2.

UOM: 1 * 100 µl

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Supplier: SIGMA ALDRICH MICROSCOPY

Description: It may be used to prepare porphyrin based matrices for the detection of water soluble vitamins by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry. It may be used to prepare 5,10,15,20-tetrakis (4-polyethyleneoxy)phenyl)) porphyrin. Nanoporous silica inserted with 2H-OHTPP imparts gas sensitivity, and it could be useful to detect NO2 by surface plasmon resonance.

Catalog Number: (BOSSBS-11246R-A350)

Supplier: Bioss

Description: In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunit have been identified, designated PP1, PP2A, PP2B and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4), is a putative member of a novel PP family. The PP2B family comprises subfamily members PP2B-A alpha, PP2B-A Beta and PP2B-A Gamma. Two additional regulatory subunits been identified, designated PP2B-B1 and PP2B-B2.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-10342R-A555)

Supplier: Bioss

Description: In eukaryotes, the phosphorylation and dephosphorylation of proteins on serine and threonine residues is an essential means of regulating a broad range of cellular functions including division, homeostasis and apoptosis. A group of proteins that are intimately involved in this process are the protein phosphatases. In general, the protein phosphatase (PP) holoenzyme is a trimeric complex composed of a regulatory subunit, a variable subunit and a catalytic subunit. Four major families of protein phosphatase catalytic subunit have been identified, designated PP1, PP2A, PP2B and PP2C. An additional protein phosphatase catalytic subunit, PPX (also known as PP4), is a putative member of a novel PP family. The PP2B family comprises subfamily members PP2B-A alpha, PP2B-A Beta and PP2B-A Gamma. Two additional regulatory subunits been identified, designated PP2B-B1 and PP2B-B2.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11281R-CY5)

Supplier: Bioss

Description: The Eph subfamily represents the largest group of receptor protein tyrosine kinases identified to date (1–3). While the biological activities of these receptors have yet to be determined, there is increasing evidence that they are involved in central nervous system function and in development (1–3). The Eph subfamily receptors of human origin (and their murine/avian homologs) include EphA1 (Eph), EphA2 (Eck), EphA3 (Hek4), EphA4 (Hek8), EphA5 (Hek7), EphA6 (Hek12), EphA7 (Hek11/MDK1), EphA8 (Hek3), EphB1 (Hek6), EphB2 (Hek5), EphB3 (Cek10, Hek2), EphB4 (Htk), EphB5 (Hek9) and EphB6 (Mep). Ligands for Eph receptors include ephrin-A4 (LERK-4) which binds EphA3 and EphB1. In addition, ephrin-A2 (ELF-1) has been described as the ligand for EphA4, ephrin-A3 (Ehk1-L) as the ligand for EphA5 and ephrin-B2 (Htk-L) as the ligand for EphB4 (Htk) (4–7).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11281R-CY7)

Supplier: Bioss

Description: The Eph subfamily represents the largest group of receptor protein tyrosine kinases identified to date (1–3). While the biological activities of these receptors have yet to be determined, there is increasing evidence that they are involved in central nervous system function and in development (1–3). The Eph subfamily receptors of human origin (and their murine/avian homologs) include EphA1 (Eph), EphA2 (Eck), EphA3 (Hek4), EphA4 (Hek8), EphA5 (Hek7), EphA6 (Hek12), EphA7 (Hek11/MDK1), EphA8 (Hek3), EphB1 (Hek6), EphB2 (Hek5), EphB3 (Cek10, Hek2), EphB4 (Htk), EphB5 (Hek9) and EphB6 (Mep). Ligands for Eph receptors include ephrin-A4 (LERK-4) which binds EphA3 and EphB1. In addition, ephrin-A2 (ELF-1) has been described as the ligand for EphA4, ephrin-A3 (Ehk1-L) as the ligand for EphA5 and ephrin-B2 (Htk-L) as the ligand for EphB4 (Htk) (4–7).

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11333R-CY3)

Supplier: Bioss

Description: Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with Clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of Clathrin binding Adaptin proteins (g and b1 for AP-1, a and b2 for AP-2) and two smaller subunits known as AP50 and AP17. The a and b Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. a-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP-3 (also designated AP180 or F1-20) is a synapse-specific Clathrin assembly protein. The protein CALM (Clathrin assembly protein lymphoid myeloid leukemia) is highly homologous to AP180 and may also be involved in Clathrin assembly.

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Catalog Number: (BOSSBS-11333R-CY5)

Supplier: Bioss

Description: Clathrin-coated pits and vesicles are assembled for receptor-mediated endocytosis through interaction with Clathrin associated protein complexes. Vesicle transport is mediated from the trans-Golgi network by the adapter complex AP-1 and from the plasma membrane by the AP-2 complex. The AP-1 and AP-2 adapter protein complexes consist of Clathrin binding Adaptin proteins (g and b1 for AP-1, a and b2 for AP-2) and two smaller subunits known as AP50 and AP17. The a and b Adaptin chains have a similar two-domain organization with C-terminal domains that vary in both sequence and length. a-Adaptin splice variants A and C display variable relative expression levels and differential distribution in different tissues. AP-3 (also designated AP180 or F1-20) is a synapse-specific Clathrin assembly protein. The protein CALM (Clathrin assembly protein lymphoid myeloid leukemia) is highly homologous to AP180 and may also be involved in Clathrin assembly.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-12933R)

Supplier: Bioss

Description: Chymotrypsins are digestive enzymes that can perform proteolysis by cleaving peptides at the carboxyl side of tyrosine, tryptophan, leucine and phenylalanine, although over time they can also hydrolyze other amide bonds, especially those with leucine-donated carboxyls. Chymotrypsins cleave peptide bonds by attacking the non-reactive carbonyl group with a powerful nucleophile, which momentarily becomes covalently bonded to the substrate to form an intermediate. Chymotrypsin B (CTRB1) and Chymotrypsin B2 (CTRB2) are synthesized in the pancreas by protein biosynthesis as precursors that are enzymatically inactive, but become active as three polypeptide molecules that are interconnected by disulfide bonds.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11470R-A647)

Supplier: Bioss

Description: Plexins are a family of large, transmembrane receptors for multiple classes of semaphorins in vertebrates. They are widely expressed, and regions of their extracellular domain are homologus to both scatter factor receptors and semaphorin domains. Plexins may act as semaphorin receptors alone or in combination with neuropilins. Plexins are divided into four subfamilies designated plexin-A, -B, -C, and -D. Plexin-B1 and -B2 are both receptors for Sema4D, which stimulates axonal outgrowth of embryonic dorsal root ganglion neurons. . Plexin-B3 binds to Sema5A, which controls axon guidance and can initiate the intracellular signaling of the hepatocyte growth factor/scatter factor receptor Met.

UOM: 1 * 100 µl

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Catalog Number: (BOSSBS-11281R-A647)

Supplier: Bioss

Description: The Eph subfamily represents the largest group of receptor protein tyrosine kinases identified to date (1–3). While the biological activities of these receptors have yet to be determined, there is increasing evidence that they are involved in central nervous system function and in development (1–3). The Eph subfamily receptors of human origin (and their murine/avian homologs) include EphA1 (Eph), EphA2 (Eck), EphA3 (Hek4), EphA4 (Hek8), EphA5 (Hek7), EphA6 (Hek12), EphA7 (Hek11/MDK1), EphA8 (Hek3), EphB1 (Hek6), EphB2 (Hek5), EphB3 (Cek10, Hek2), EphB4 (Htk), EphB5 (Hek9) and EphB6 (Mep). Ligands for Eph receptors include ephrin-A4 (LERK-4) which binds EphA3 and EphB1. In addition, ephrin-A2 (ELF-1) has been described as the ligand for EphA4, ephrin-A3 (Ehk1-L) as the ligand for EphA5 and ephrin-B2 (Htk-L) as the ligand for EphB4 (Htk) (4–7).

UOM: 1 * 100 µl

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Supplier: Apollo Scientific

Description: D-(+)-Biotin 99%

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